|Gene:||aes||Accession Numbers: EG11101 (EcoCyc), b0476, ECK0470|
Aes catalyzes hydrolysis of p-nitrophenyl esters of fatty acids, preferring substrates with short (<8 in length) acyl chains [Kanaya98]. Aes binds to the maltose operon regulator, MalT, and inhibits MalT transcriptional activation activity in competition with its inducer, maltotriose [Joly02]. Residues in MalT that are important for binding of Aes have been identified [Schlegel02a], and structure-based alanine scanning mutagenesis has identified residues in Aes that are responsible for interaction with MalT [Schiefner13]. Aes also binds to α-galactosidase; this interaction stimulates Aes esterase activity and inhibits α-galactosidase, suggesting that Aes may have a physiological role in regulation of metabolism of carbohydrates [Mandrich02]. Other proteins that interact with Aes have been identified [DAmbrosio08].
Aes has similarity to lipases and esterases [Peist97] and belongs to the hormone-sensitive lipase (HSL) protein family [Kanaya98]. The enzyme may be either monomeric [Kanaya98] or homodimeric [Schiefner13]; it has been crystallized [Sorrentino03, Gerber04], and crystal structures have been solved [Schiefner13]. Denaturant-induced unfolding of the enzyme has been studied [Del04], and a mutant with higher thermostability has been isolated [Farias07]. The catalytic triad was predicted to comprise Ser165, Asp262, and His292 [Kanaya98]; site-directed mutagenesis confirmed that these residues are required for catalytic activity. In addition, Asp164 is thought to be structurally important [Haruki99]. Point mutations in L97 and L209 increase enzymatic activity by increasing kcat and decreasing Km, respectively [Kobayashi12].
Overexpression of aes results in increased p-nitrophenyl acetate hydrolysis, compared to wild type, and this strain shows growth on triacetyl glycerol and repression of the maltose transport system [Peist97]. A genetic interaction between malT and aes has been observed [Peist97]. Mutations in MalT have differential effects on the sensitivity of MalT to Aes and MalY, which inhibit the activator in similar, yet distinct, ways [Joly02, Schlegel02a].
Aes is identical to esterase B, a protein marker used to distinguish E. coli phylogenetic groups [Lescat09].
Aes: "acetyl esterase" [Peist97]
|Map Position: [498,238 <- 499,197] (10.74 centisomes)||Length: 960 bp / 319 aa|
Molecular Weight of Polypeptide: 36.034 kD (from nucleotide sequence), 37.0 kD (experimental) [Peist97 ]
Unification Links: ASAP:ABE-0001651 , DIP:DIP-9062N , EchoBASE:EB1093 , EcoGene:EG11101 , EcoliWiki:b0476 , ModBase:P23872 , OU-Microarray:b0476 , PortEco:aes , PR:PRO_000022064 , Protein Model Portal:P23872 , RefSeq:NP_415009 , RegulonDB:EG11101 , SMR:P23872 , String:511145.b0476 , UniProt:P23872
Relationship Links: InterPro:IN-FAMILY:IPR002168 , InterPro:IN-FAMILY:IPR013094 , InterPro:IN-FAMILY:IPR023508 , PDB:Structure:4KRX , PDB:Structure:4KRY , Pfam:IN-FAMILY:PF07859 , Prosite:IN-FAMILY:PS01173 , Prosite:IN-FAMILY:PS01174
|Biological Process:||GO:0043433 - negative regulation of sequence-specific DNA binding transcription factor activity
GO:0051346 - negative regulation of hydrolase activity [Mandrich02]
GO:0008152 - metabolic process [GOA01a]
|Molecular Function:||GO:0005515 - protein binding
GO:0008126 - acetylesterase activity [Kanaya98]
GO:0016787 - hydrolase activity [UniProtGOA11a, GOA01a, Kanaya98]
GO:0034338 - short-chain carboxylesterase activity [Kanaya98]
GO:0042803 - protein homodimerization activity [Schiefner13]
GO:0052689 - carboxylic ester hydrolase activity [UniProtGOA11a, GOA06, GOA01a]
|Cellular Component:||GO:0005737 - cytoplasm
[UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, Kanaya98]
GO:0005829 - cytosol [DiazMejia09]
|MultiFun Terms:||metabolism → carbon utilization → carbon compounds|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB enriched||Yes||37||Aerobic||6.95||Yes [Gerdes03, Comment 1]|
|LB Lennox||Yes||37||Aerobic||7||Yes [Baba06, Comment 2]|
|M9 medium with 1% glycerol||Yes||37||Aerobic||7.2||0.35||Yes [Joyce06, Comment 3]|
|MOPS medium with 0.4% glucose||Yes||37||Aerobic||7.2||0.22||Yes [Baba06, Comment 2]|
Enzymatic reaction of: acetyl esterase
Synonyms: acetyl-esterase, acetylesterase
EC Number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown.
Kinetic parameters for various p-nitrophenyl esters of fatty acids have been measured [Kanaya98].
Note that acetyl-esterase is unstable at its optimal temperature [Farias07].
T(opt): 65 °C [Farias07]
|Protein-Segment||91 -> 93|
|Sequence-Conflict||275 -> 319|
10/20/97 Gene b0476 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11101; confirmed by SwissProt match.
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
DAmbrosio08: D'Ambrosio C, Mandrich L, Rossi M, Scaloni A, Manco G (2008). "A proteomic approach to study Escherichia coli. Acetyl esterase interactors unveil a sequence motif involved in protein-protein interaction." Protein Pept Lett 15(4);333-40. PMID: 18473943
Del03: Del Vecchio P, Graziano G, Granata V, Barone G, Mandrich L, Rossi M, Manco G (2003). "Effect of trifluoroethanol on the conformational stability of a hyperthermophilic esterase: a CD study." Biophys Chem 104(2);407-15. PMID: 12878309
Del04: Del Vecchio P, Graziano G, Granata V, Farias T, Barone G, Mandrich L, Rossi M, Manco G (2004). "Denaturant-induced unfolding of the acetyl-esterase from Escherichia coli." Biochemistry 43(46);14637-43. PMID: 15544334
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Gerber04: Gerber K, Schiefner A, Seige P, Diederichs K, Boos W, Welte W (2004). "Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 60(Pt 3);531-3. PMID: 14993683
Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938
Haruki99: Haruki M, Oohashi Y, Mizuguchi S, Matsuo Y, Morikawa M, Kanaya S (1999). "Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis." FEBS Lett 454(3);262-6. PMID: 10431819
Joly02: Joly N, Danot O, Schlegel A, Boos W, Richet E (2002). "The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon." J Biol Chem 277(19);16606-13. PMID: 11867639
Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394
Khersonsky11: Khersonsky O, Malitsky S, Rogachev I, Tawfik DS (2011). "Role of chemistry versus substrate binding in recruiting promiscuous enzyme functions." Biochemistry 50(13);2683-90. PMID: 21332126
Kobayashi12: Kobayashi R, Hirano N, Kanaya S, Haruki M (2012). "Enhancement of the enzymatic activity of Escherichia coli acetyl esterase by a double mutation obtained by random mutagenesis." Biosci Biotechnol Biochem 76(11);2082-8. PMID: 23132590
Lescat09: Lescat M, Hoede C, Clermont O, Garry L, Darlu P, Tuffery P, Denamur E, Picard B (2009). "aes, the gene encoding the esterase B in Escherichia coli, is a powerful phylogenetic marker of the species." BMC Microbiol 9;273. PMID: 20040078
Mandrich02: Mandrich L, Caputo E, Martin BM, Rossi M, Manco G (2002). "The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism." J Biol Chem 277(50);48241-7. PMID: 12374803
Miyamoto91: Miyamoto K, Nakahigashi K, Nishimura K, Inokuchi H (1991). "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12." J Mol Biol 219(3);393-8. PMID: 2051480
Peist97: Peist R, Koch A, Bolek P, Sewitz S, Kolbus T, Boos W (1997). "Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity." J Bacteriol 179(24);7679-86. PMID: 9401025
Schlegel02a: Schlegel A, Danot O, Richet E, Ferenci T, Boos W (2002). "The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY." J Bacteriol 184(11);3069-77. PMID: 12003949
Sorrentino03: Sorrentino N, De Simone G, Menchise V, Mandrich L, Rossi M, Manco G, Pedone C (2003). "Crystallization and preliminary X-ray diffraction studies of Aes acetyl-esterase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 59(Pt 10);1846-8. PMID: 14501134
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493